Identification of TMEM206 proteins as pore of PAORAC/ASOR acid-sensitive chloride channels

Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channe...

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Published ineLife Vol. 8
Main Authors Ullrich, Florian, Blin, Sandy, Lazarow, Katina, Daubitz, Tony, von Kries, Jens Peter, Jentsch, Thomas J
Format Journal Article
LanguageEnglish
Published England eLife Science Publications, Ltd 18.07.2019
eLife Sciences Publications Ltd
eLife Sciences Publications, Ltd
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Online AccessGet full text
ISSN2050-084X
2050-084X
DOI10.7554/eLife.49187

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Abstract Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR’s pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR’s role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed.
AbstractList Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR's pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR's role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed.
Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR's pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR's role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed.Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR's pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR's role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed.
Audience Academic
Author Lazarow, Katina
von Kries, Jens Peter
Blin, Sandy
Jentsch, Thomas J
Daubitz, Tony
Ullrich, Florian
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  fullname: Lazarow, Katina
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  orcidid: 0000-0002-3509-2553
  surname: Jentsch
  fullname: Jentsch, Thomas J
  organization: Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany, Max-Delbrück-Centrum für Molekulare Medizin (MDC), Berlin, Germany, NeuroCure Cluster of Excellence, Charité Universitätsmedizin, Berlin, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31318332$$D View this record in MEDLINE/PubMed
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Keywords acidotoxicity
naked mole rat
PAC
cell biology
Cl- channel
proton-activated
ICl,H
structural biology
molecular biophysics
human
Language English
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Snippet Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained...
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SubjectTerms Acidification
Acidity
acidotoxicity
Acids
Acids - metabolism
Animals
Anions - metabolism
Apoptosis
Cell Biology
Cell death
Cell Death - genetics
Cell Membrane - genetics
Cell Membrane - metabolism
Cell membranes
Channel pores
Chloride
Chloride channels
Chloride Channels - chemistry
Chloride Channels - genetics
Chloride Channels - metabolism
Chlorides - metabolism
Cl- channel
Genetic screening
Genome, Human - genetics
Genomes
Genomics
HeLa Cells
Humans
Hydrogen-Ion Concentration
ICl,H
Identification and classification
Ion channels
Membrane proteins
naked mole rat
Novels
PAC
Physiological aspects
Proteins
proton-activated
Protons
RNA
siRNA
Sodium channels
Structural Biology and Molecular Biophysics
Transmembrane domains
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Title Identification of TMEM206 proteins as pore of PAORAC/ASOR acid-sensitive chloride channels
URI https://www.ncbi.nlm.nih.gov/pubmed/31318332
https://www.proquest.com/docview/2267349894
https://www.proquest.com/docview/2259917908
https://pubmed.ncbi.nlm.nih.gov/PMC6663466
https://doaj.org/article/b4e93c9d6cbd4a358027e742c7171744
Volume 8
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